Skip to main content

Thank you for visiting nature.com. You are using a browser version with limited support for CSS. To obtain the best experience, we recommend you use a more up to date browser (or turn off compatibility mode in Internet Explorer). In the meantime, to ensure continued support, we are displaying the site without styles and JavaScript.

  • Letter
  • Published:

Oxygen Dissociation of Sheep Haemoglobins A and B in Solution

Nature volume 211, pages 533–534 (1966)Cite this article

Abstract

Two distinct electrophoretic types of sheep haemoglobin have been identified by Harris and Warren1. They designated the fast-moving component which travelled towards the anode at pH. 8.6 ‘haemoglobin A’, and the slow-moving one ‘haemoglobin B’ Similar electrophoretic differences were found with adult haemoglobins in Dutch sheep by Helm at al.2, which they named HbI and HbII, corresponding to HbB and HbA respectively. Further differences in chromatographic behaviour, in resistance to denaturation by alkali, in solubility in concentrated salt solutions and in amino-acid composition were demonstrated for HbI and HbII2. The oxygen equilibrium curves of these haemoglobins were also found to be different3,4, HbII(A) having a higher affinity for oxygen than Hbl(B), and it has been suggested that HbII(A) originated in sheep living at high altitude.

Access through your institution
Buy or subscribe

This is a preview of subscription content, access via your institution

Access options

Access through your institution

Buy this article

  • Purchase on SpringerLink
  • Instant access to full article PDF
Buy now

Prices may be subject to local taxes which are calculated during checkout

Similar content being viewed by others

References

  1. Harris, H., and Warren, F. L., Biochem. J., 60, 29 (1955).

    Google Scholar 

  2. Helm, H. J. van der, Vliet, G. van, and Huisman, T. H. J., Arch. Biochem. Biophys., 72, 331 (1957).

    Article  Google Scholar 

  3. Huisman, T. H. J., Vliet, G. van, and Sebens, T., Nature, 182, 171 (1958).

    Article  ADS  CAS  Google Scholar 

  4. Kernohan, J. C., J. Physiol., 155, 580 (1961).

    Article  CAS  Google Scholar 

  5. Gibson, Q. H., and Roughton, F. J. W., Proc. Roy. Soc., B, 143, 310 (1955).

    ADS  CAS  Google Scholar 

  6. Gibson, Q. H., and Roughton, F. J. W., J. Physiol., 145, 32P (1959).

    Google Scholar 

  7. Kernohan, J. C., J. Physiol., 145, 32P (1959).

    Google Scholar 

  8. Roughton, F. J. W., Legge, J. W., and Nicolson, P., Haemoglobin (Barcroft Memorial Conference), 67 (Butterworths Scientific Publications, London, 1949).

    Google Scholar 

  9. Dalziel, >K., and O'Brien, J. R. P., Biochem. J., 49, xlvii (1951).

Download references

Author information

Authors and Affiliations

  1. Department of Physics, St. Mary's Hospital Medical School, London, W.2

    JOHN A. SIRS

Authors
  1. JOHN A. SIRS
    View author publications

    Search author on:PubMed Google Scholar

Rights and permissions

Reprints and permissions

About this article

Cite this article

SIRS, J. Oxygen Dissociation of Sheep Haemoglobins A and B in Solution. Nature 211, 533–534 (1966). https://doi.org/10.1038/211533b0

Download citation

  • Issue date:

  • DOI: https://doi.org/10.1038/211533b0

Search

Advanced search

Quick links

Nature Briefing

Sign up for the Nature Briefing newsletter — what matters in science, free to your inbox daily.

Get the most important science stories of the day, free in your inbox. Sign up for Nature Briefing